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Conserved domains on  [gi|2024343403|ref|XP_004934770|]
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oral-facial-digital syndrome 1 protein isoform X2 [Gallus gallus]

Protein Classification

kinesin family protein; PEPP family PH domain-containing protein( domain architecture ID 13870895)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain| PEPP (phosphoinositol 3-phosphate-binding protein) family PH (pleckstrin homology) domain-containing protein similar to PH domain region of vertebrate pleckstrin homology domain-containing family A member 4/5/6/7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-469 1.33e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQL-----QAE-------MSQKLQHfKEVEVAKIKME----EKAQTQKEISELRYELER--THQAKAEALVSREK 217
Cdd:COG1196   195 LGELERQLeplerQAEkaeryreLKEELKE-LEAELLLLKLReleaELEELEAELEELEAELEEleAELAELEAELEELR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 218 NAIERLQKQQEIEAKEVYAQRQS---LLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY 294
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 295 DQKLKtELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNK 374
Cdd:COG1196   354 EEAEA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 375 QNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES 454
Cdd:COG1196   433 LEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
                         330
                  ....*....|....*
gi 2024343403 455 HKQFLEKQLQSEVER 469
Cdd:COG1196   510 VKAALLLAGLRGLAG 524
LisH_2 pfam16045
LisH;
27-52 1.98e-10

LisH;


:

Pssm-ID: 464992  Cd Length: 28  Bit Score: 56.31  E-value: 1.98e-10
                          10        20
                  ....*....|....*....|....*.
gi 2024343403  27 NSLVADHLQRCGYEYSLSVFFPESGL 52
Cdd:pfam16045   2 NSLIAEYLQSQGYNYTLSVFLPESGL 27
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-469 1.33e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQL-----QAE-------MSQKLQHfKEVEVAKIKME----EKAQTQKEISELRYELER--THQAKAEALVSREK 217
Cdd:COG1196   195 LGELERQLeplerQAEkaeryreLKEELKE-LEAELLLLKLReleaELEELEAELEELEAELEEleAELAELEAELEELR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 218 NAIERLQKQQEIEAKEVYAQRQS---LLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY 294
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 295 DQKLKtELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNK 374
Cdd:COG1196   354 EEAEA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 375 QNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES 454
Cdd:COG1196   433 LEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
                         330
                  ....*....|....*
gi 2024343403 455 HKQFLEKQLQSEVER 469
Cdd:COG1196   510 VKAALLLAGLRGLAG 524
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
187-507 1.94e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 1.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  187 KAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQE--IEAKEVYAQRQSLLKDIEVMRTReaELKQRIEAFEI 264
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaERYKELKAELRELELALLVLRLE--ELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  265 TQKLQEEKNKTIDDALRRREVAVkNIEETYDQKLKTELLKYQLELKEEYIartnkvtedekknkekamllreeavAVNSK 344
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALAN-------------------------EISRL 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  345 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 424
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEELESLEAELEELEAELEELESRL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  425 SQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEkQLQSEVERSAQLKTQLLD--SEATVRKLNVQVEDLKLQLKQTQ 502
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQ 453

                   ....*
gi 2024343403  503 AALEN 507
Cdd:TIGR02168  454 EELER 458
LisH_2 pfam16045
LisH;
27-52 1.98e-10

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 56.31  E-value: 1.98e-10
                          10        20
                  ....*....|....*....|....*.
gi 2024343403  27 NSLVADHLQRCGYEYSLSVFFPESGL 52
Cdd:pfam16045   2 NSLIAEYLQSQGYNYTLSVFLPESGL 27
PTZ00121 PTZ00121
MAEBL; Provisional
125-541 5.07e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 5.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  125 AEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE---KAQTQKEISELRYEL 201
Cdd:PTZ00121  1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKA 1479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  202 ErtHQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEvmRTREAELKQRIEAFEITQKLQEEKNKTIDDALR 281
Cdd:PTZ00121  1480 E--EAKKADEA---KKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  282 RREvAVKNIEEtydqKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVnsKKEELKQAvsrtKELELD 361
Cdd:PTZ00121  1553 KAE-ELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKA----EEAKIK 1621
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  362 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLR--DKLSQPSAEHLACQA-EL 438
Cdd:PTZ00121  1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALKKEAeEA 1701
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  439 RKVEHSRRLVMDEFESHKQfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDL-KLQLKQTQAALENEVYRNPKPSL 517
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkKIAHLKKEEEKKAEEIRKEKEAV 1780
                          410       420
                   ....*....|....*....|....
gi 2024343403  518 VDRSVIDLIDDRIVPHDVYTDSIF 541
Cdd:PTZ00121  1781 IEEELDEEDEKRRMEVDKKIKDIF 1804
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
151-481 8.73e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.05  E-value: 8.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  151 KLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELerthqakAEALVSREKNAIERLQKQQEIE 230
Cdd:pfam02463  177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-------YLDYLKLNEERIDLLQELLRDE 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  231 AKEVYAQRQSLLKDIEVMRTREAELKQRIEAfeitQKLQEEKNKTIDDAL------RRREVAVKNIEETYDQKLKTELLK 304
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKE----KKLQEEELKLLAKEEeelkseLLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  305 YQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESvKAQVLLVNKQNQLLTEKLK 384
Cdd:pfam02463  326 AEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-ERLSSAAKLKEEELELKSE 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  385 EVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQ 464
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-ELKKSEDLLKETQLVK 481
                          330
                   ....*....|....*..
gi 2024343403  465 SEVERSAQLKTQLLDSE 481
Cdd:pfam02463  482 LQEQLELLLSRQKLEER 498
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
154-441 1.14e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIEKQLQAEMSQ----KLQHFKEVEVAKIKMEE---KAQTQKEISELRY--------ELERTHQ-----------A 207
Cdd:NF033838  114 ELTSKTKKELDAAFEQfkkdTLEPGKKVAEATKKVEEaekKAKDQKEEDRRNYptntyktlELEIAESdvevkkaelelV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 208 KAEALVSREKNAIErlQKQQEIEAKEVYAQRqslLKDIEVMRTR-EAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA 286
Cdd:NF033838  194 KEEAKEPRDEEKIK--QAKAKVESKKAEATR---LEKIKTDREKaEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 287 VKNIEETYDQKlKTELLKYQLELKEEYIARTN-----KVTEDEKKnkekamlLREEAVAVNSKKEELKQAVSRTKELELD 361
Cdd:NF033838  269 VLGEPATPDKK-ENDAKSSDSSVGEETLPSPSlkpekKVAEAEKK-------VEEAKKKAKDQKEEDRRNYPTNTYKTLE 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQNQLLTEKLKEVSDypllkEEKLElQVQNKLLRQQLDETRTENqhLRDKLSQPSAEHLACQAELRKV 441
Cdd:NF033838  341 LEIAESDVKVKEAELELVKEEAKEPRN-----EEKIK-QAKAKVESKKAEATRLEK--IKTDRKKAEEEAKRKAAEEDKV 412
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
27-54 7.33e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.10  E-value: 7.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 2024343403   27 NSLVADHLQRCGYEYSLSVFFPESGLEK 54
Cdd:smart00667   7 NRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-469 1.33e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQL-----QAE-------MSQKLQHfKEVEVAKIKME----EKAQTQKEISELRYELER--THQAKAEALVSREK 217
Cdd:COG1196   195 LGELERQLeplerQAEkaeryreLKEELKE-LEAELLLLKLReleaELEELEAELEELEAELEEleAELAELEAELEELR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 218 NAIERLQKQQEIEAKEVYAQRQS---LLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY 294
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 295 DQKLKtELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNK 374
Cdd:COG1196   354 EEAEA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 375 QNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES 454
Cdd:COG1196   433 LEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
                         330
                  ....*....|....*
gi 2024343403 455 HKQFLEKQLQSEVER 469
Cdd:COG1196   510 VKAALLLAGLRGLAG 524
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
148-448 1.43e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRkEIEKQLQAEMSQKLQHFKEVEVAKikmEEKAQTQKEISELRYELER-----THQAKAEALVSREKNAIER 222
Cdd:COG1196   227 AELLLLKLR-ELEAELEELEAELEELEAELEELE---AELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTel 302
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-- 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 303 lkyQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEK 382
Cdd:COG1196   381 ---LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 383 LKEVSDyPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLV 448
Cdd:COG1196   458 EEALLE-LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
187-507 1.94e-10

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.08  E-value: 1.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  187 KAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQE--IEAKEVYAQRQSLLKDIEVMRTReaELKQRIEAFEI 264
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaERYKELKAELRELELALLVLRLE--ELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  265 TQKLQEEKNKTIDDALRRREVAVkNIEETYDQKLKTELLKYQLELKEEYIartnkvtedekknkekamllreeavAVNSK 344
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALAN-------------------------EISRL 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  345 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 424
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEELESLEAELEELEAELEELESRL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  425 SQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEkQLQSEVERSAQLKTQLLD--SEATVRKLNVQVEDLKLQLKQTQ 502
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQ 453

                   ....*
gi 2024343403  503 AALEN 507
Cdd:TIGR02168  454 EELER 458
LisH_2 pfam16045
LisH;
27-52 1.98e-10

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 56.31  E-value: 1.98e-10
                          10        20
                  ....*....|....*....|....*.
gi 2024343403  27 NSLVADHLQRCGYEYSLSVFFPESGL 52
Cdd:pfam16045   2 NSLIAEYLQSQGYNYTLSVFLPESGL 27
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
120-412 1.71e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 120 YRESLAEKLQLIDEQFADsypqhhkyepLEGKLHEYRKEIEkQLQAEMSQ-KLQHFKEVEVAKIKMEEKAQTQKEISELR 198
Cdd:COG1196   233 KLRELEAELEELEAELEE----------LEAELEELEAELA-ELEAELEElRLELEELELELEEAQAEEYELLAELARLE 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 199 YELERTHQAKAEALVSREKNAIERLQKQQEIEAKEvyAQRQSLLKDIEvmrTREAELKQRIEAFEITQKLQEEKNKTIDD 278
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELE--EELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAE 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 279 ALRRREVAVKNIEEtydqkLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKEL 358
Cdd:COG1196   377 AEEELEELAEELLE-----ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024343403 359 ELDLESVKAQVLLVNKQNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDE 412
Cdd:COG1196   452 AELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEAD 502
PTZ00121 PTZ00121
MAEBL; Provisional
125-541 5.07e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 5.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  125 AEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE---KAQTQKEISELRYEL 201
Cdd:PTZ00121  1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKA 1479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  202 ErtHQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEvmRTREAELKQRIEAFEITQKLQEEKNKTIDDALR 281
Cdd:PTZ00121  1480 E--EAKKADEA---KKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  282 RREvAVKNIEEtydqKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVnsKKEELKQAvsrtKELELD 361
Cdd:PTZ00121  1553 KAE-ELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKA----EEAKIK 1621
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  362 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLR--DKLSQPSAEHLACQA-EL 438
Cdd:PTZ00121  1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALKKEAeEA 1701
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  439 RKVEHSRRLVMDEFESHKQfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDL-KLQLKQTQAALENEVYRNPKPSL 517
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkKIAHLKKEEEKKAEEIRKEKEAV 1780
                          410       420
                   ....*....|....*....|....
gi 2024343403  518 VDRSVIDLIDDRIVPHDVYTDSIF 541
Cdd:PTZ00121  1781 IEEELDEEDEKRRMEVDKKIKDIF 1804
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
144-506 7.78e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 59.70  E-value: 7.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  144 KYEPLEGKLHEYRKEIEKqLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELertHQAKAEALVsREKNAIERL 223
Cdd:TIGR02169  171 KKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYE---LLKEKEALE-RQKEAIERQ 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  224 QKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRI------EAFEITQKLQEEKNK--TIDDALRRREVAVKNIEETyD 295
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEER-L 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  296 QKLKTELLKYQLELK------EEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSK----KEELKQAVSRTKELELDLESV 365
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEelereiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKLKREINEL 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  366 KAQVLLVNKQNQLLTEKLKEV-SDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHS 444
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024343403  445 RRLVMDEFEShkqfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:TIGR02169  485 LSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
151-487 1.13e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  151 KLHEYRKEIEKQLQA-------------EMSQKLQHFK-EVEVAKIKMEEKAQ-TQKEISELRYELERTHQAKAEALVSR 215
Cdd:TIGR02168  169 KYKERRKETERKLERtrenldrledilnELERQLKSLErQAEKAERYKELKAElRELELALLVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  216 EKNAIERLQKQQEIEAKEvyaqrqsllKDIEVMRTREAELKQRIE----AFEITQKLQEEKNKTIDDALRRREVAVKNIE 291
Cdd:TIGR02168  249 KEAEEELEELTAELQELE---------EKLEELRLEVSELEEEIEelqkELYALANEISRLEQQKQILRERLANLERQLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  292 ETYDQKL----KTELLKYQLELKEEYIARTNKVTED-EKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVK 366
Cdd:TIGR02168  320 ELEAQLEelesKLDELAEELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  367 AQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELqvQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRR 446
Cdd:TIGR02168  400 NEIERLEARLERLEDRRER------LQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2024343403  447 LVMDEFESHKQFLEkQLQSEVERSAQLKTQLLDSEATVRKL 487
Cdd:TIGR02168  472 EAEQALDAAERELA-QLQARLDSLERLQENLEGFSEGVKAL 511
PTZ00121 PTZ00121
MAEBL; Provisional
144-523 4.27e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  144 KYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKA---EALVSREKNAI 220
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadEAKKAEEAKKA 1524
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  221 ERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY-----D 295
Cdd:PTZ00121  1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyeeE 1604
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  296 QKLKTELLKYQLELKEEyiARTNKVTEDEKKNKEKAMLLREEAVavnSKKEELKQAvsrtkelELDLESVKAQVLLVNKQ 375
Cdd:PTZ00121  1605 KKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKA-------EEENKIKAAEEAKKAEE 1672
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  376 NQLLTEKLKevsdypllKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESH 455
Cdd:PTZ00121  1673 DKKKAEEAK--------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024343403  456 KQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVedLKLQLKQTQAALENEVYRNPKPSLVDRSVI 523
Cdd:PTZ00121  1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-500 4.30e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 4.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  189 QTQKEISELRYELERThQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKL 268
Cdd:TIGR02168  674 ERRREIEELEEKIEEL-EEKIAEL---EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  269 QEEkNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELK-EEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEE 347
Cdd:TIGR02168  750 AQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  348 LKQAVSRTK----ELELDLESVKAQVLLVNKQ-NQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRD 422
Cdd:TIGR02168  829 LERRIAATErrleDLEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403  423 KLSQPSAEHLACQAELRKVEhsrrLVMDEFESHKQFLEKQLQSEVERSAQ-LKTQLLDSEATVRKLNVQVEDLKLQLKQ 500
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKE 983
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
124-387 7.83e-08

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 56.40  E-value: 7.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 124 LAEKLQLIDEQFADSYPQHHKYEP-LEGKLHEYRKEIEKQLQ-----AEMSQKLQHFKEVEVAKIKMEEKAQTQK----- 192
Cdd:PLN03229  484 LQERLENLREEFSKANSQDQLMHPvLMEKIEKLKDEFNKRLSrapnyLSLKYKLDMLNEFSRAKALSEKKSKAEKlkaei 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 193 -----------EISE----LRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVYaqrQSLLKDIEVMRTREAELKQ 257
Cdd:PLN03229  564 nkkfkevmdrpEIKEkmeaLKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVL---KSMGLEVIGVTKKNKDTAE 640
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 258 RIEAFEITQK---LQEEKNKTIDDALRrrevavknieeTYDQKLKTELLKyqLELKEEyiARTNKVTEDEKKNKEKAMLL 334
Cdd:PLN03229  641 QTPPPNLQEKiesLNEEINKKIERVIR-----------SSDLKSKIELLK--LEVAKA--SKTPDVTEKEKIEALEQQIK 705
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024343403 335 REEAVAVNSKkeELKQavsrtKELELDLESVKAQVLLVNKQNQLLTEKLKEVS 387
Cdd:PLN03229  706 QKIAEALNSS--ELKE-----KFEELEAELAAARETAAESNGSLKNDDDKEED 751
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
151-481 8.73e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.05  E-value: 8.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  151 KLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELerthqakAEALVSREKNAIERLQKQQEIE 230
Cdd:pfam02463  177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-------YLDYLKLNEERIDLLQELLRDE 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  231 AKEVYAQRQSLLKDIEVMRTREAELKQRIEAfeitQKLQEEKNKTIDDAL------RRREVAVKNIEETYDQKLKTELLK 304
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKE----KKLQEEELKLLAKEEeelkseLLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  305 YQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESvKAQVLLVNKQNQLLTEKLK 384
Cdd:pfam02463  326 AEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-ERLSSAAKLKEEELELKSE 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  385 EVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQ 464
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-ELKKSEDLLKETQLVK 481
                          330
                   ....*....|....*..
gi 2024343403  465 SEVERSAQLKTQLLDSE 481
Cdd:pfam02463  482 LQEQLELLLSRQKLEER 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
141-387 1.57e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  141 QHHKYEPLEGKLHEY---RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERT---HQAKAEALVS 214
Cdd:TIGR02168  237 LREELEELQEELKEAeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  215 REKNAIERLQ--KQQEIEAKEVYAQRQsllKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEE 292
Cdd:TIGR02168  317 QLEELEAQLEelESKLDELAEELAELE---EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  293 T-YDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMlLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLL 371
Cdd:TIGR02168  394 QiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250
                   ....*....|....*.
gi 2024343403  372 VNKQNQLLTEKLKEVS 387
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
122-477 1.59e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 122 ESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLqAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYEL 201
Cdd:PRK03918  227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 202 ERTHQaKAEALVSREKNAIERLQKQ-QEIEAKEvyAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNK------ 274
Cdd:PRK03918  306 LDELR-EIEKRLSRLEEEINGIEERiKELEEKE--ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrlt 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 275 --TIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKeeyIARTNKVTEDEKKNK-------------EKAMLLREEAV 339
Cdd:PRK03918  383 glTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE---IKELKKAIEELKKAKgkcpvcgrelteeHRKELLEEYTA 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 340 AVNSKKEELKQAVSRTKELELDLESVKAqvlLVNKQNQLLteKLKEVSDYPLLKEEKLElqvqnKLLRQQLDETRTENQH 419
Cdd:PRK03918  460 ELKRIEKELKEIEEKERKLRKELRELEK---VLKKESELI--KLKELAEQLKELEEKLK-----KYNLEELEKKAEEYEK 529
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024343403 420 LRDKLSQPSAEHLACQAELRKVEhsrrlvmdEFESHKQFLEKQLQSEVERSAQLKTQL 477
Cdd:PRK03918  530 LKEKLIKLKGEIKSLKKELEKLE--------ELKKKLAELEKKLDELEEELAELLKEL 579
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
184-479 1.69e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  184 MEEKAQTQKEISELRYELERTHQ-------------AKAEALVSREKNAIERLQK-QQEIEAKEvyAQRQSLLKDIEVMR 249
Cdd:TIGR02169  694 QSELRRIENRLDELSQELSDASRkigeiekeieqleQEEEKLKERLEELEEDLSSlEQEIENVK--SELKELEARIEELE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  250 TREAELKQRIEAFE------ITQKLQEEKNKtIDDALRRREVAVKNIE---------ETYDQKLKTELLKYQLELKEEYI 314
Cdd:TIGR02169  772 EDLHKLEEALNDLEarlshsRIPEIQAELSK-LEEEVSRIEARLREIEqklnrltleKEYLEKEIQELQEQRIDLKEQIK 850
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  315 ARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKaqvllvNKQNQLLTEKLKEVSDYPLLKE 394
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE------RKIEELEAQIEKKRKRLSELKA 924
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  395 EKLELQVQNKLLRQQLDETRTENQHLRDkLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLeKQLQSEVERSAQLK 474
Cdd:TIGR02169  925 KLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEER 1002

                   ....*
gi 2024343403  475 TQLLD 479
Cdd:TIGR02169 1003 KAILE 1007
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
159-470 2.64e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 159 IEKQLQAEMSQKLQHFKEVEVAKIKmEEKAQTQKEIsELRYELERTHQAKAEAL-------VSREKNAIERLQKQQEIEA 231
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLR-QEKEEKAREV-ERRRKLEEAEKARQAEMdrqaaiyAEQERMAMERERELERIRQ 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 232 KEvyaqrqsllKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA--VKNIEETYDQKLKTELLKYQLEL 309
Cdd:pfam17380 356 EE---------RKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArkVKILEEERQRKIQQQKVEMEQIR 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 310 KEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDY 389
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 390 PLLKEEKLELQVQNKLLRQQL----DETRTENQHLRDKlSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQS 465
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKaiyeEERRREAEEERRK-QQEMEERRRIQEQMRKATEERSR-LEAMEREREMMRQIVES 584

                  ....*
gi 2024343403 466 EVERS 470
Cdd:pfam17380 585 EKARA 589
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
253-508 4.44e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 253 AELKQRIEAFEItQKLQEEKNKTIDDALRRREV--AVKNIEETydQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEK 330
Cdd:COG1196   196 GELERQLEPLER-QAEKAERYRELKEELKELEAelLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEEL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 331 AMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKaqvllvnKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQL 410
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEE------LEEELAELEEELEELEEEL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 411 DETRTENQHLRDKLSQPSAEHLACQAELRKVE---HSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKL 487
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEAEaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                         250       260
                  ....*....|....*....|.
gi 2024343403 488 NVQVEDLKLQLKQTQAALENE 508
Cdd:COG1196   420 EEELEELEEALAELEEEEEEE 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-508 5.45e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRKEIEKQLQaEMSQKLQHFKEVE-VAKIKMEEKAQTQKEISELRYELERTHQAKAEalVSREKNAIER 222
Cdd:PRK03918  159 DYENAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEeLIKEKEKELEEVLREINEISSELPELREELEK--LEKEVKELEE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQkqQEIEAKEVyaQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKtiddalrrrevaVKNIEETYDQKLKTEL 302
Cdd:PRK03918  236 LK--EEIEELEK--ELESLEGSKRKLEEKIRELEERIE--ELKKEIEELEEK------------VKELKELKEKAEEYIK 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 303 LKyqlELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEK 382
Cdd:PRK03918  298 LS---EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 383 LKevsdyplLKEEKLELQVQNklLRQQLDETRTENQHLRDKLSQPSAEhlacQAELRKVEHSRRLVMDEFESHKQF--LE 460
Cdd:PRK03918  375 ER-------LKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITAR----IGELKKEIKELKKAIEELKKAKGKcpVC 441
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024343403 461 KQLQSEVERS---AQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALENE 508
Cdd:PRK03918  442 GRELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE 492
PTZ00121 PTZ00121
MAEBL; Provisional
149-359 6.64e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 6.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  149 EGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE--KAQTQKEISELRY--ELERTHQAKAEALV-SREKNAIERL 223
Cdd:PTZ00121  1204 AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakKAEEERNNEEIRKfeEARMAHFARRQAAIkAEEARKADEL 1283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  224 QKQQEIEAKEvYAQRQSLLKDIEVMRTREAELKQRIEA---FEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKT 300
Cdd:PTZ00121  1284 KKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403  301 ELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE 359
Cdd:PTZ00121  1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
148-506 6.84e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVakiKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQ 227
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEE---ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 228 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQ- 306
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEe 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 307 LELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQA-------------VSRTKELELDLESVKAQVLLV- 372
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLVl 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 373 ----------NKQNQLLTEKLKEVSDYPLLKE-EKLELQVQNKLLRQQLDETRTENQHLRDKLSQ-----PSAEHLACQA 436
Cdd:COG4717   284 gllallflllAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEElqellREAEELEEEL 363
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403 437 ELRKVEHSRRLVMDEF--ESHKQFLEK-----QLQSEVERSAQLKTQLLDSEATVRKLNVQV--EDLKLQLKQTQAALE 506
Cdd:COG4717   364 QLEELEQEIAALLAEAgvEDEEELRAAleqaeEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELE 442
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-500 1.15e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  91 LMWILMGLTEHHLSKECNDRETQTISIPpyrESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIE--KQLQAEMS 168
Cdd:COG4717    39 LLAFIRAMLLERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 169 QKLQHFKEVEVAKIKMEEKAQTQKEISEL--RYE-LERTHQAKAEALVSREKNAIERLQKQQEIEAK------EVYAQRQ 239
Cdd:COG4717   116 EELEKLEKLLQLLPLYQELEALEAELAELpeRLEeLEERLEELRELEEELEELEAELAELQEELEELleqlslATEEELQ 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 240 SLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKEEYIARTNK 319
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 320 ------------VTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRT--KELELDLESVKAQVLLVNKQNQLLTEKLKE 385
Cdd:COG4717   276 agvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQELLRE 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 386 VSDYpllkEEKLELQVQNKLLRQQLDETRTENqhlRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQS 465
Cdd:COG4717   356 AEEL----EEELQLEELEQEIAALLAEAGVED---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2024343403 466 EV-ERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQ 500
Cdd:COG4717   429 ELeEELEELEEELEELEEELEELREELAELEAELEQ 464
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
185-512 3.40e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  185 EEKAQTQKEISELRYELERTHQakaealvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEI 264
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQS---------ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  265 TQKLQEEKNKTIDDALRRREvavKNIEEtydqkLKTELLKYQLELkeeyiartnkvtedekkNKEKAMLLREEAVAVNSK 344
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELE---ARIEE-----LEEDLHKLEEAL-----------------NDLEARLSHSRIPEIQAE 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  345 KEELKQAVSRtkeLELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 424
Cdd:TIGR02169  800 LSKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEIQE------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  425 sqpsAEHlacQAELRKVEHSRrlvmdefeshkqfleKQLQSEVERsaqLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAA 504
Cdd:TIGR02169  871 ----EEL---EAALRDLESRL---------------GDLKKERDE---LEAQLRELERKIEELEAQIEKKRKRLSELKAK 925

                   ....*...
gi 2024343403  505 LENEVYRN 512
Cdd:TIGR02169  926 LEALEEEL 933
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
156-297 4.71e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.76  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEAlvSREKNAIERLQKQQEIEAK--- 232
Cdd:TIGR02794  83 QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA--EAERKAKEEAAKQAEEEAKaka 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343403 233 --EVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQK 297
Cdd:TIGR02794 161 aaEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
PRK12704 PRK12704
phosphodiesterase; Provisional
266-420 7.43e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 266 QKLQEEKNKTIDDALRRREVAVKNIEetydQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKK 345
Cdd:PRK12704   34 KEAEEEAKRILEEAKKEAEAIKKEAL----LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 346 EELKQAVSRTKELELDLESVKAQV-LLVNKQNQllteKLKEVSDypLLKEEklelqVQNKLLRQQLDETRTENQHL 420
Cdd:PRK12704  110 EELEKKEKELEQKQQELEKKEEELeELIEEQLQ----ELERISG--LTAEE-----AKEILLEKVEEEARHEAAVL 174
PRK12704 PRK12704
phosphodiesterase; Provisional
149-313 9.62e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAEmsqklqhfkEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQ---- 224
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEA---------KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldr 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 225 KQQEIEAKE--VYAQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKTIDDAlrrREVAVKNIEEtydqKLKTEL 302
Cdd:PRK12704  101 KLELLEKREeeLEKKEKELEQKQQELEKKEEELEELIE--EQLQELERISGLTAEEA---KEILLEKVEE----EARHEA 171
                         170
                  ....*....|.
gi 2024343403 303 LKYQLELKEEY 313
Cdd:PRK12704  172 AVLIKEIEEEA 182
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-495 1.62e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRK---EIEKQLqAEMSQKLQHFKE-VEVAKIKMEEKAQTQKEISELRYELERTHQ-AKAEALVSREKN 218
Cdd:PRK03918  294 EYIKLSEFYEEYLDelrEIEKRL-SRLEEEINGIEErIKELEEKEERLEELKKKLKELEKRLEELEErHELYEEAKAKKE 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 219 AIERLQKQQEIEAKEvyaqrqSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNktiddalrRREVAVKNIEETYDQKL 298
Cdd:PRK03918  373 ELERLKKRLTGLTPE------KLEKELEELEKAKEEIEEEIS--KITARIGELKK--------EIKELKKAIEELKKAKG 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 299 KTELLKYQL------ELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEE------LKQAVSRTKELE-----LD 361
Cdd:PRK03918  437 KCPVCGRELteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEeklkkYN 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLA-CQAELRK 440
Cdd:PRK03918  517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKE 596
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343403 441 VE--HSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLK 495
Cdd:PRK03918  597 LEpfYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
100-508 1.85e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.34  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  100 EHHLSKECNDRETQTISIppyrESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQL---------------- 163
Cdd:TIGR00618  378 TQHIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQryaelcaaaitctaqc 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  164 -------QAEMSQKL----QHFKEVEVAKIKMEEK-------AQTQKEI------SELRYELERTHQAKAEALVSREKNA 219
Cdd:TIGR00618  454 eklekihLQESAQSLkereQQLQTKEQIHLQETRKkavvlarLLELQEEpcplcgSCIHPNPARQDIDNPGPLTRRMQRG 533
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  220 IERLQKQQEIEAKeVYAQRQSLLKDIEVMRTREAELKQRIEAFEIT-QKLQEEKNKTIDDALRRREVAVKNIEEtydQKL 298
Cdd:TIGR00618  534 EQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCdNRSKEDIPNLQNITVRLQDLTEKLSEA---EDM 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  299 KTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLRE-EAVAVNSKKEELKQAVSRTKELELDLesvkaqvllvNKQNQ 377
Cdd:TIGR00618  610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLTLTQERVREHALSIRVLPKEL----------LASRQ 679
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  378 LLTEKLKevSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES--- 454
Cdd:TIGR00618  680 LALQKMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvlk 757
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024343403  455 HKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALENE 508
Cdd:TIGR00618  758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
169-402 2.03e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 45.30  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 169 QKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERT----------HQAKAEALVSREKNAIERLQKQQEIEAKEVYAQR 238
Cdd:PRK05771   23 EALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklrsylpkLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 239 QSLLKDIEVMRTREAELKQRIEAFEITQKLqeeknkTIDDA-LRRRE---VAVKNIEETYDqklktELLKYQLELKEEYI 314
Cdd:PRK05771  103 KELEEEISELENEIKELEQEIERLEPWGNF------DLDLSlLLGFKyvsVFVGTVPEDKL-----EELKLESDVENVEY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 315 ARTNK-------VTEDEKKNKEKAMLLREEAVAVN-----SKKEELKQAVSRTKELELDLESVKAQvllvnkqnqlLTEK 382
Cdd:PRK05771  172 ISTDKgyvyvvvVVLKELSDEVEEELKKLGFERLEleeegTPSELIREIKEELEEIEKERESLLEE----------LKEL 241
                         250       260
                  ....*....|....*....|
gi 2024343403 383 LKEVSDYPLLKEEKLELQVQ 402
Cdd:PRK05771  242 AKKYLEELLALYEYLEIELE 261
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
146-507 3.20e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.83  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  146 EPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVeVAKIKMEEKAQTQKeISELRYELE------------RTHQAKAEA-- 211
Cdd:pfam12128  271 ETLIASRQEERQETSAELNQLLRTLDDQWKEK-RDELNGELSAADAA-VAKDRSELEaledqhgafldaDIETAAADQeq 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  212 --LVSREKNAIER-----LQKQQEIEAKevYAQRQSLLK-----DIEVMR-----TREAELKQRIEAFEITQKLQEEKNK 274
Cdd:pfam12128  349 lpSWQSELENLEErlkalTGKHQDVTAK--YNRRRSKIKeqnnrDIAGIKdklakIREARDRQLAVAEDDLQALESELRE 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  275 TIDDALRRREVAVKNIEET-------YDQKLKTELLKYQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVA---VNSK 344
Cdd:pfam12128  427 QLEAGKLEFNEEEYRLKSRlgelklrLNQATATPELLLQLENFDERIERARE--EQEAANAEVERLQSELRQArkrRDQA 504
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  345 KEELKQAVSRTKELELDLESVKAQvlLVNKQNQLLTEKLKEVSDYpllKEEKLELQVQNKLLRQQLDETRTEnqhlrdkl 424
Cdd:pfam12128  505 SEALRQASRRLEERQSALDELELQ--LFPQAGTLLHFLRKEAPDW---EQSIGKVISPELLHRTDLDPEVWD-------- 571
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  425 SQPSAEH--LACQAELRKVEHSRRLVM-DEFESHKQFLEKQLQSEVERSAQLKTQLLdseatvrKLNVQVEDLKLQLKQT 501
Cdd:pfam12128  572 GSVGGELnlYGVKLDLKRIDVPEWAASeEELRERLDKAEEALQSAREKQAAAEEQLV-------QANGELEKASREETFA 644

                   ....*.
gi 2024343403  502 QAALEN 507
Cdd:pfam12128  645 RTALKN 650
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
148-507 3.35e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.63  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRKEIE---KQLQAEMSQKLQHF-KEVEVAKIKMEEK-AQTQKEISELRYELERTHQAKAEALVSREKNAIER 222
Cdd:TIGR04523 286 LEKQLNQLKSEISdlnNQKEQDWNKELKSElKNQEKKLEEIQNQiSQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQKQQEIEakEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNI-EETYDQKLKTE 301
Cdd:TIGR04523 366 EEKQNEIE--KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLkETIIKNNSEIK 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 302 LLKYQLELKEEYIARTNKVTEDEKKNKEKAML--------LREEAVAVNSKKEELKQAVSRTKELELDLESVKAQV-LLV 372
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsSLK 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 373 NKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKllRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVehsrrlvMDEF 452
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL-------IDQK 594
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024343403 453 ESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALEN 507
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
PTZ00121 PTZ00121
MAEBL; Provisional
145-474 3.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  145 YEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRyeleRTHQAKAEALVSREKNAIERLQ 224
Cdd:PTZ00121  1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR----KAEDAKRVEIARKAEDARKAEE 1168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  225 KQQEIEAKEVYAQRqsllKDIEVMRT---REAELKQRIEA---FEITQKLQE----EKNKTIdDALRRREVAVKNIEETY 294
Cdd:PTZ00121  1169 ARKAEDAKKAEAAR----KAEEVRKAeelRKAEDARKAEAarkAEEERKAEEarkaEDAKKA-EAVKKAEEAKKDAEEAK 1243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  295 ---DQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTK----------ELELD 361
Cdd:PTZ00121  1244 kaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkaeeakkadEAKKK 1323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  362 LESVKAQVLLVNKQnqllTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKV 441
Cdd:PTZ00121  1324 AEEAKKKADAAKKK----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2024343403  442 EHSRRLVMDEFEshKQFLEKQLQSEVERSAQLK 474
Cdd:PTZ00121  1400 AEEDKKKADELK--KAAAAKKKADEAKKKAEEK 1430
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
154-506 3.43e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  154 EYRKEIE---KQLQAEMSQKL-------QHFKEVEVAKIKMEEKAQTQKE-ISELRYELERTHQAKAEALVSREKnaiER 222
Cdd:pfam01576  650 EAKEELErtnKQLRAEMEDLVsskddvgKNVHELERSKRALEQQVEEMKTqLEELEDELQATEDAKLRLEVNMQA---LK 726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  223 LQKQQEIEAKEVYAQ--RQSLLKDIEVMRT-REAELKQRIEAFEITQKLQ---EEKNKTIDDALRRREVAVKNIeetydQ 296
Cdd:pfam01576  727 AQFERDLQARDEQGEekRRQLVKQVRELEAeLEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAVKQL-----K 801
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  297 KLKTELLKYQLELKEEYIAR-----TNKVTEDEKKNKEKAMLLREEAVAVNSKKEelKQAVSRTKEL--ELDLESVKAQV 369
Cdd:pfam01576  802 KLQAQMKDLQRELEEARASRdeilaQSKESEKKLKNLEAELLQLQEDLAASERAR--RQAQQERDELadEIASGASGKSA 879
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  370 LLVNKQN------QLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEH 443
Cdd:pfam01576  880 LQDEKRRleariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343403  444 SRR----LVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:pfam01576  960 TVKskfkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
148-387 3.53e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRKEIEkqlQAEmsQKLQHFKE----VEVAkikmEEKAQTQKEISELRYELERTHQAKAEAlvsreKNAIERL 223
Cdd:COG3206   180 LEEQLPELRKELE---EAE--AALEEFRQknglVDLS----EEAKLLLQQLSELESQLAEARAELAEA-----EARLAAL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 224 QKQQEIEAKEVYAQRQSLLkdIEVMRTREAELKQRIEafEITQKLQEEkNKTIDDALRRREVAvknieetyDQKLKTELL 303
Cdd:COG3206   246 RAQLGSGPDALPELLQSPV--IQQLRAQLAELEAELA--ELSARYTPN-HPDVIALRAQIAAL--------RAQLQQEAQ 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 304 KYQLELKEEYIArtnkvtedekknkekamlLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKL 383
Cdd:COG3206   313 RILASLEAELEA------------------LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374

                  ....
gi 2024343403 384 KEVS 387
Cdd:COG3206   375 EEAR 378
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-494 4.70e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVY 235
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 236 AQRQSLLKDIEVMRTREAELKQRIEAfEITQKLQEEKNKTIDDALRRREVAVKNIEET----YDQKLKTELLKYQLELKE 311
Cdd:COG1196   517 AGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARG 595
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 312 EYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPL 391
Cdd:COG1196   596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 392 LKEEKLELQVQ-----NKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQSE 466
Cdd:COG1196   676 EAEAELEELAErlaeeELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                         330       340
                  ....*....|....*....|....*...
gi 2024343403 467 VERSAQLKTQlldsEATVRKLNVQVEDL 494
Cdd:COG1196   756 LPEPPDLEEL----ERELERLEREIEAL 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-495 4.94e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRKEIEKQLQ------AEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREK 217
Cdd:PRK03918  311 EIEKRLSRLEEEINGIEERIKeleekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 218 NAIERLQKQQEieakEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQ--------KLQEEKNKTIddaLRRREVAVKN 289
Cdd:PRK03918  391 KELEELEKAKE----EIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKEL---LEEYTAELKR 463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 290 IEETY------DQKLKTELLKYQLELKEEYIARTNKVTEDE----------------KKNKEKAMLLREEAVAVNSKKEE 347
Cdd:PRK03918  464 IEKELkeieekERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleelEKKAEEYEKLKEKLIKLKGEIKS 543
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 348 LKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEV--SDYPLLKEEKLELQ------VQNKLLRQQLDETRTENQH 419
Cdd:PRK03918  544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfESVEELEERLKELEpfyneyLELKDAEKELEREEKELKK 623
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 420 LRDKLSQPSAEHLACQAELRKV-----EHSRRLVMDEFESHKQF---LEKQLQSEVERSAQLKTQLLDSEATVRKLNVQV 491
Cdd:PRK03918  624 LEEELDKAFEELAETEKRLEELrkeleELEKKYSEEEYEELREEyleLSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703

                  ....
gi 2024343403 492 EDLK 495
Cdd:PRK03918  704 EERE 707
PTZ00121 PTZ00121
MAEBL; Provisional
124-388 5.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 5.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  124 LAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELER 203
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  204 THQAKAEALVSREKNAIERLQKQQEIEAKEVyaqrqsllkdiEVMRTREAELKQRIEAFeitqKLQEEKNKTIDDALRRR 283
Cdd:PTZ00121  1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----------EELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKE 1738
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  284 EvavkniEEtydQKLKTELLKYQLELKeeyiartNKVTEDEKKNKEKAMLLREEAVAV---NSKKEELKQAVSRTKELEl 360
Cdd:PTZ00121  1739 A------EE---DKKKAEEAKKDEEEK-------KKIAHLKKEEEKKAEEIRKEKEAVieeELDEEDEKRRMEVDKKIK- 1801
                          250       260
                   ....*....|....*....|....*...
gi 2024343403  361 DLESVKAQVLLVNKQNQLLTEKLKEVSD 388
Cdd:PTZ00121  1802 DIFDNFANIIEGGKEGNLVINDSKEMED 1829
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
185-416 5.98e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 185 EEKAQTQKEISELRYELERTHQAKAEALvsREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAfei 264
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALL--KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA--- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 265 tqkLQEEKNKTIDDALRR----REVAVKNIEETYDQKLKTELLKYQLElkeeyiartnkvtedekKNKEKAMLLREEAVA 340
Cdd:COG4942   102 ---QKEELAELLRALYRLgrqpPLALLLSPEDFLDAVRRLQYLKYLAP-----------------ARREQAEELRADLAE 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 341 VNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKevSDYPLLKEEKLELQVQNKLLRQQLDETRTE 416
Cdd:COG4942   162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAE 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
142-506 7.30e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 142 HHKYEPLEGKLHEYRKEIEKQlqaeMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREkNAIE 221
Cdd:PRK02224  205 HERLNGLESELAELDEEIERY----EEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERERE-ELAE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 222 RLQKQQEiEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFeitqklqEEKNKTIDDALRRREVAVKNIEETYDqklkte 301
Cdd:PRK02224  280 EVRDLRE-RLEELEEERDDLLAEAGLDDADAEAVEARREEL-------EDRDEELRDRLEECRVAAQAHNEEAE------ 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 302 llkyqlelkeeyiartnKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAV----SRTKELELDLESVKAQVllvnkqnQ 377
Cdd:PRK02224  346 -----------------SLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF-------G 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 378 LLTEKLKEVSDY-PLLKEEKLELQVQNKLLR---QQLDETRTENQHLRDKLSQPSaehlaCQAELRKVEHSRRLVMDEfe 453
Cdd:PRK02224  402 DAPVDLGNAEDFlEELREERDELREREAELEatlRTARERVEEAEALLEAGKCPE-----CGQPVEGSPHVETIEEDR-- 474
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024343403 454 shkqflekqlqsevERSAQLKTQLLDSEATVRKLNVQVEDLKlQLKQTQAALE 506
Cdd:PRK02224  475 --------------ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE 512
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
121-472 8.69e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 8.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  121 RESLAEKLQLIDEQFAdsypqhhkyeplegkLHEYRKEIEKQ--LQAEMSQKLQ----HFKEVEVAKIKMEEKAQTQKEI 194
Cdd:COG3096    292 RELFGARRQLAEEQYR---------------LVEMARELEELsaRESDLEQDYQaasdHLNLVQTALRQQEKIERYQEDL 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  195 SELRYELERTHQAKAEALVSREKNAIERLQKQQEI-EAKEVYAQRQSLLkdiEVMRTREAELKQRIEAFEITQKLQEEKN 273
Cdd:COG3096    357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdSLKSQLADYQQAL---DVQQTRAIQYQQAVQALEKARALCGLPD 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  274 KTIDDALRRREVAVKNIEETYDQKLKtelLKYQLELKEEYIARTNKVTE---------DEKKNKEKAMLLREEAVAVNSK 344
Cdd:COG3096    434 LTPENAEDYLAAFRAKEQQATEEVLE---LEQKLSVADAARRQFEKAYElvckiagevERSQAWQTARELLRRYRSQQAL 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  345 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKE------EKLELQVQNKL-----LRQQLDET 413
Cdd:COG3096    511 AQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAeleaqlEELEEQAAEAVeqrseLRQQLEQL 590
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403  414 RTENQHLRDK-------------LSQPSAEHLACQAEL-----RKVEHSRRLVM--DEFESHKQflekQLQSEVERSAQ 472
Cdd:COG3096    591 RARIKELAARapawlaaqdalerLREQSGEALADSQEVtaamqQLLEREREATVerDELAARKQ----ALESQIERLSQ 665
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
154-441 1.14e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIEKQLQAEMSQ----KLQHFKEVEVAKIKMEE---KAQTQKEISELRY--------ELERTHQ-----------A 207
Cdd:NF033838  114 ELTSKTKKELDAAFEQfkkdTLEPGKKVAEATKKVEEaekKAKDQKEEDRRNYptntyktlELEIAESdvevkkaelelV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 208 KAEALVSREKNAIErlQKQQEIEAKEVYAQRqslLKDIEVMRTR-EAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA 286
Cdd:NF033838  194 KEEAKEPRDEEKIK--QAKAKVESKKAEATR---LEKIKTDREKaEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 287 VKNIEETYDQKlKTELLKYQLELKEEYIARTN-----KVTEDEKKnkekamlLREEAVAVNSKKEELKQAVSRTKELELD 361
Cdd:NF033838  269 VLGEPATPDKK-ENDAKSSDSSVGEETLPSPSlkpekKVAEAEKK-------VEEAKKKAKDQKEEDRRNYPTNTYKTLE 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQNQLLTEKLKEVSDypllkEEKLElQVQNKLLRQQLDETRTENqhLRDKLSQPSAEHLACQAELRKV 441
Cdd:NF033838  341 LEIAESDVKVKEAELELVKEEAKEPRN-----EEKIK-QAKAKVESKKAEATRLEK--IKTDRKKAEEEAKRKAAEEDKV 412
COG5022 COG5022
Myosin heavy chain [General function prediction only];
152-497 2.74e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  152 LHEYRKEIEKQLqaEMSQKLQhfkevevakiKMEEKAQTQKEiselRYELERTHqaKAEALVSREKNAIERLQKQQEIEA 231
Cdd:COG5022    805 LLGSRKEYRSYL--ACIIKLQ----------KTIKREKKLRE----TEEVEFSL--KAEVLIQKFGRSLKAKKRFSLLKK 866
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  232 KEVYAQRQSLLKDIevmRTREAELKQRIEAFEITQKLQEEKNKTIddalrrrevavknIEETydQKLKTELLKyQLELKE 311
Cdd:COG5022    867 ETIYLQSAQRVELA---ERQLQELKIDVKSISSLKLVNLELESEI-------------IELK--KSLSSDLIE-NLEFKT 927
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  312 EYIARtnkvtedEKKNKEKAML--LREEAVAVNSKKEELKQAVSRTKELELDLESvkaqvlLVNKQNQLLTEKLKEVSDY 389
Cdd:COG5022    928 ELIAR-------LKKLLNNIDLeeGPSIEYVKLPELNKLHEVESKLKETSEEYED------LLKKSTILVREGNKANSEL 994
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  390 PLLKEEKLELQVQNKLLR---QQLDETRTENQHLRDKLSQPSAEHLACQAELrKVEHSRRLVMDEFESHKQFLeKQLQSE 466
Cdd:COG5022    995 KNFKKELAELSKQYGALQestKQLKELPVEVAELQSASKIISSESTELSILK-PLQKLKGLLLLENNQLQARY-KALKLR 1072
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2024343403  467 VERSAQLKTQLLDSEATVRKLN-VQVEDLKLQ 497
Cdd:COG5022   1073 RENSLLDDKQLYQLESTENLLKtINVKDLEVT 1104
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
126-480 2.91e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 126 EKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQlQAEMSQKLQH-----FKEVEVAKIKMEEKAQTQKEISELRYE 200
Cdd:COG5185   236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGE-NAESSKRLNEnannlIKQFENTKEKIAEYTKSIDIKKATESL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 201 LERTHQAKAEALVSREKNAIErlqkqqeieaKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLqEEKNKTIDDAL 280
Cdd:COG5185   315 EEQLAAAEAEQELEESKRETE----------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL-SKSSEELDSFK 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 281 RRREVAVKNIeetyDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELEl 360
Cdd:COG5185   384 DTIESTKESL----DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD- 458
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 361 dlesvkaqvllvNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNklLRQQLDETRTENQHLRDKLSQPSaehlacqAELRK 440
Cdd:COG5185   459 ------------EESQSRLEEAYDEINRSVRSKKEDLNEELTQ--IESRVSTLKATLEKLRAKLERQL-------EGVRS 517
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2024343403 441 VEHSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDS 480
Cdd:COG5185   518 KLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAK 557
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
154-511 3.08e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  154 EYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE-KAQTQKEISELRYELERTH---------QAKAEALVSREKNAIERL 223
Cdd:pfam01576  541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtKNRLQQELDDLLVDLDHQRqlvsnlekkQKKFDQMLAEEKAISARY 620
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  224 QKQQ---EIEAKEVYAQRQSLLKDIEvmrtreaELKQRIEAFEITQKLQEEKnktIDDALRRREVAVKNIE--------- 291
Cdd:pfam01576  621 AEERdraEAEAREKETRALSLARALE-------EALEAKEELERTNKQLRAE---MEDLVSSKDDVGKNVHelerskral 690
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  292 ETYDQKLKTELLKYQLELKEEYIAR------------------TNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVS 353
Cdd:pfam01576  691 EQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA 770
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  354 RTKELELDLESVKAQVLLVNKQNQLLTEKLKevsdypllkeeklELQVQNKLLRQQLDETR-------TENQHLRDKLSQ 426
Cdd:pfam01576  771 AKKKLELDLKELEAQIDAANKGREEAVKQLK-------------KLQAQMKDLQRELEEARasrdeilAQSKESEKKLKN 837
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  427 PSAEHLACQAELRKVEHSRRLVMDEFEshkqflekQLQSEVERSAQLKTQLLDSEatvRKLNVQVEDLKLQLKQTQAALE 506
Cdd:pfam01576  838 LEAELLQLQEDLAASERARRQAQQERD--------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELEEEQSNTE 906

                   ....*..
gi 2024343403  507 --NEVYR 511
Cdd:pfam01576  907 llNDRLR 913
PRK09039 PRK09039
peptidoglycan -binding protein;
393-506 3.18e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 393 KEEKL-ELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLV---MDEFESHKQFLEKQLQSEVE 468
Cdd:PRK09039   51 KDSALdRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELagaGAAAEGRAGELAQELDSEKQ 130
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2024343403 469 RSAQLKTQlldseatVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:PRK09039  131 VSARALAQ-------VELLNQQIAALRRQLAALEAALD 161
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
121-502 3.44e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  121 RESLAEKLQLIDEQFADSypqhhkyEPLEGKLHEYRKEIEKQLQaEMSQKLQhfKEVEVAKIKMEEKAQTQKEISELRYE 200
Cdd:pfam01576   42 KNALQEQLQAETELCAEA-------EEMRARLAARKQELEEILH-ELESRLE--EEEERSQQLQNEKKKMQQHIQDLEEQ 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  201 LERTHQAKAEalVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELK-QRIEAFEITQKLQEEKNK---TI 276
Cdd:pfam01576  112 LDEEEAARQK--LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEKAKSLSKLKNKheaMI 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  277 DDALRRREVAVKNIEETydQKLKTELLKYQLELKEEYIARTNKVTE----DEKKNKE-KAMLLR--EEAVAVNSKKEELK 349
Cdd:pfam01576  190 SDLEERLKKEEKGRQEL--EKAKRKLEGESTDLQEQIAELQAQIAElraqLAKKEEElQAALARleEETAQKNNALKKIR 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  350 QAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEkLELQVQNKLLRQQLDETR-TENQHLRDKLSQPS 428
Cdd:pfam01576  268 ELEAQISELQEDLESERAARNKAEKQRRDLGEELEA------LKTE-LEDTLDTTAAQQELRSKReQEVTELKKALEEET 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  429 AEHLACQAELRKvEHSRRLV-----MDEFESHKQFLEKQLQSEVERSAQLKTQL-------LDSEATVRKLNVQVEDLKL 496
Cdd:pfam01576  341 RSHEAQLQEMRQ-KHTQALEelteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQA 419

                   ....*.
gi 2024343403  497 QLKQTQ 502
Cdd:pfam01576  420 RLSESE 425
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
206-509 3.62e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 206 QAKAEALVSRE--KNAIERLQKQQEIEAKEVYAQR--QSLLKDIEVMRTREAEL-------KQRIEAFEITQKLQEEknk 274
Cdd:COG3206    84 ETQIEILKSRPvlERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVieisytsPDPELAAAVANALAEA--- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 275 TIDDALRRREVAVKNIEETYDQKLKTelLKYQLELKEEYIARTnkvtedekKNKEKAMLLREEAVAVNSKKEELKQAVSr 354
Cdd:COG3206   161 YLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEEF--------RQKNGLVDLSEEAKLLLQQLSELESQLA- 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 355 tkELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPL---LKEEKLELQVQnkllRQQLDETRTEN----QHLRDKLSQp 427
Cdd:COG3206   230 --EARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqLRAQLAELEAE----LAELSARYTPNhpdvIALRAQIAA- 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 428 saehlacqaelrkvehsrrlvmdefeshkqfLEKQLQSEVERS-AQLKTQLLDSEATVRKLNVQVEDLKLQLK------Q 500
Cdd:COG3206   303 -------------------------------LRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAelpeleA 351

                  ....*....
gi 2024343403 501 TQAALENEV 509
Cdd:COG3206   352 ELRRLEREV 360
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
135-354 3.67e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 135 FADSYPQHHKYEPLEGKLHEYRKEI---EKQLQAEMSQKLQHFKEVEVAKIKMeekAQTQKEISELRYELERThQAKAEA 211
Cdd:COG4942    12 ALAAAAQADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAAL-EAELAE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 212 LVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDD-ALRRREVAVKNI 290
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAALRA 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024343403 291 EETYDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSR 354
Cdd:COG4942   168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
122-475 4.79e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 122 ESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQT-QKEISELRYE 200
Cdd:COG4717   142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAElEEELEEAQEE 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 201 LERTHQAkaealVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFE-------ITQKLQEEKN 273
Cdd:COG4717   222 LEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllALLFLLLARE 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 274 KTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKEEYIArtnkVTEDEKKNKEkamlLREEAVAVNSKKEELKQAVS 353
Cdd:COG4717   297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE----LLELLDRIEE----LQELLREAEELEEELQLEEL 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 354 RTKELEL-------DLESVKAQVLLVNKQNQlLTEKLKEVSDY--PLLKEEKLELQVQNK-LLRQQLDETRTENQHLRDK 423
Cdd:COG4717   369 EQEIAALlaeagveDEEELRAALEQAEEYQE-LKEELEELEEQleELLGELEELLEALDEeELEEELEELEEELEELEEE 447
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024343403 424 LSQPSAEHLACQAELRKVEHSRRLvmDEFESHKQFLEKQLQSEVERSAQLKT 475
Cdd:COG4717   448 LEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKL 497
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
180-356 4.84e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 40.70  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 180 AKIKMEEKAQTQKEISELRYE-----LERT-------HQAKAEALVSREKN----AIERLQKQQEIEAKEVYAQRQSLLK 243
Cdd:PRK05035  436 AEIRAIEQEKKKAEEAKARFEarqarLEREkaarearHKKAAEARAAKDKDavaaALARVKAKKAAATQPIVIKAGARPD 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 244 DIEVMRTREAELKQRIEAFEITQKLQEE--KNKTIDDALRR--------REVAVKNIEETYDQKLKTEL------LKYQL 307
Cdd:PRK05035  516 NSAVIAAREARKAQARARQAEKQAAAAAdpKKAAVAAAIARakakkaaqQAANAEAEEEVDPKKAAVAAaiarakAKKAA 595
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343403 308 ELKEEYIARTNKVTEDEKKNKEKAMLLR------------EEAVAVNSKKEELKQAVSRTK 356
Cdd:PRK05035  596 QQAASAEPEEQVAEVDPKKAAVAAAIARakakkaeqqanaEPEEPVDPRKAAVAAAIARAK 656
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
154-357 4.90e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEAlvsREKNAIERLQKQQEIEAKE 233
Cdd:PRK09510   63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA---EEAAKQAALKQKQAEEAAA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 234 VYAQRQSLLKDIEVMrtREAELKQRIEAfeitqklqEEKNKTIDDALRRREV-AVKNIEETYDQKLKTEL-LKYQLELKE 311
Cdd:PRK09510  140 KAAAAAKAKAEAEAK--RAAAAAKKAAA--------EAKKKAEAEAAKKAAAeAKKKAEAEAAAKAAAEAkKKAEAEAKK 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2024343403 312 EYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKE 357
Cdd:PRK09510  210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-263 5.06e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVY 235
Cdd:COG1196   673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
                          90       100
                  ....*....|....*....|....*...
gi 2024343403 236 AQRQSLLKDIEVMRTREAELKQRIEAFE 263
Cdd:COG1196   753 LEELPEPPDLEELERELERLEREIEALG 780
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
121-506 5.07e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 5.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  121 RESLAEKLQLIdEQFADSYPQ--HHKYEPLEGKLHEYRKEI--EKQLQAEMSQKLQhfkevevakiKMEEKAQTQKEISE 196
Cdd:TIGR00618  196 AELLTLRSQLL-TLCTPCMPDtyHERKQVLEKELKHLREALqqTQQSHAYLTQKRE----------AQEEQLKKQQLLKQ 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  197 LRYELE---------------RTHQAKAEALVSREKNAIERLQKQQEI--EAKEVYAQRQSLLKDIEVMRTREAELKQRI 259
Cdd:TIGR00618  265 LRARIEelraqeavleetqerINRARKAAPLAAHIKAVTQIEQQAQRIhtELQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  260 EAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYD----QKLKTELLKYQLELKEEYIARTNKV----TEDEKKNKEKA 331
Cdd:TIGR00618  345 RLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihtlQQQKTTLTQKLQSLCKELDILQREQatidTRTSAFRDLQG 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  332 MLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQlLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLD 411
Cdd:TIGR00618  425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  412 -----ETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvmdefeshkQFLEKQLQSEVERSAQLKTQLLDSEATVRK 486
Cdd:TIGR00618  504 cplcgSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSE---------EDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
                          410       420
                   ....*....|....*....|
gi 2024343403  487 LNVQVEDLKLQLKQTQAALE 506
Cdd:TIGR00618  575 LTQCDNRSKEDIPNLQNITV 594
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
161-369 5.42e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 161 KQLQAEMSQKLQHFKEVEvakikmEEKAQTQKEISELRYELERTHQAKAEAlvSREKNAIERLQKQQEIEAKEVYAQRQS 240
Cdd:COG4942    23 AEAEAELEQLQQEIAELE------KELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 241 LLKDIEvmrTREAELKQRIEAFEITQKLQEEK----NKTIDDALRRREV------AVKNIEETYDQKLKT-ELLKYQLEL 309
Cdd:COG4942    95 LRAELE---AQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYlkylapARREQAEELRADLAElAALRAELEA 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343403 310 KEEYIARTNKVTEDEKKNKEKAMLLREEAVA-VNSKKEELKQAVSRTKELELDLESVKAQV 369
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLArLEKELAELAAELAELQQEAEELEALIARL 232
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
150-369 5.47e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 150 GKLHEYRKEIEKQlQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNA--IERLQKQQ 227
Cdd:PRK02224  478 EELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAaeLEAEAEEK 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 228 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREvAVKNIEETYDQ---KLKT---- 300
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE-KREALAELNDErreRLAEkrer 635
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 301 -------------ELLKYQLELKEEYIArtnKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE---LDLES 364
Cdd:PRK02224  636 kreleaefdeariEEAREDKERAEEYLE---QVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEnrvEALEA 712

                  ....*
gi 2024343403 365 VKAQV 369
Cdd:PRK02224  713 LYDEA 717
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
149-506 5.86e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAemSQKLQHfkEVEVAKIKMEEKAQTQKE-ISELRYELERTHQAKAEALVSREKNaierlqKQQ 227
Cdd:pfam05483 105 ENKLQENRKIIEAQRKA--IQELQF--ENEKVSLKLEEEIQENKDlIKENNATRHLCNLLKETCARSAEKT------KKY 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 228 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIE--AFEITQKLQEEKNKtiddalrrrevaVKNIEETYDQKLKTELLKY 305
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEKMILAFEELRVQAEnaRLEMHFKLKEDHEK------------IQHLEEEYKKEINDKEKQV 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 306 QLELKEeyiartnkVTEDEKKNKEKAMLLREEAVAVNS-------KKEELKQAVSRTKELELDLESVKaqvllVNKQNQL 378
Cdd:pfam05483 243 SLLLIQ--------ITEKENKMKDLTFLLEESRDKANQleektklQDENLKELIEKKDHLTKELEDIK-----MSLQRSM 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 379 LTEKLKEVsdypllkeeklELQVQNKLLRQQLDETRTENQhlrdklsqpsaehlacqaELRKVEHSRRLVMDEFESHKQF 458
Cdd:pfam05483 310 STQKALEE-----------DLQIATKTICQLTEEKEAQME------------------ELNKAKAAHSFVVTEFEATTCS 360
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2024343403 459 LEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
141-506 6.00e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  141 QHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFkEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAI 220
Cdd:TIGR00618  480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  221 ERLQKQQEIEAKEVYA---QRQSLLKDIEVMRTR--------EAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKN 289
Cdd:TIGR00618  559 ASLKEQMQEIQQSFSIltqCDNRSKEDIPNLQNItvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  290 IEEtydQKLKTELLKYQLEL---KEEYIARTNKVTEDEK----KNKEKAMLLREEAVAvnSKKEELKQAVSRTKELELDL 362
Cdd:TIGR00618  639 QEL---ALKLTALHALQLTLtqeRVREHALSIRVLPKELlasrQLALQKMQSEKEQLT--YWKEMLAQCQTLLRELETHI 713
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  363 E-----------SVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETR-TENQHLRDKLSQPSAE 430
Cdd:TIGR00618  714 EeydrefneienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRL 793
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403  431 HLACQAELRKVEHSRRLVMDEFEshkQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:TIGR00618  794 REEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
PRK11281 PRK11281
mechanosensitive channel MscK;
204-506 6.29e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  204 THQAKAEALVSRE--KNAIERLQKQQEIEA-----KEVYAQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKTi 276
Cdd:PRK11281    27 ARAASNGDLPTEAdvQAQLDALNKQKLLEAedklvQQDLEQTLALLDKIDRQKEETEQLKQQLA--QAPAKLRQAQAEL- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  277 dDALRRREVAVKNieetydQKLKTELLKyQLElkeeyiARTNKVTEDEKKnkekamlLREEAVAVNSkkeelkQAVSRTK 356
Cdd:PRK11281   104 -EALKDDNDEETR------ETLSTLSLR-QLE------SRLAQTLDQLQN-------AQNDLAEYNS------QLVSLQT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  357 ELEldlesvKAQVLLVNKQNQL--LTEKLKEVSD--YPLLKEEKLELQVQNKLLRQQLDETRTE---NQHLRDKLSQPSA 429
Cdd:PRK11281   157 QPE------RAQAALYANSQRLqqIRNLLKGGKVggKALRPSQRVLLQAEQALLNAQNDLQRKSlegNTQLQDLLQKQRD 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  430 EHLACQAELRK-------VEHSRRLVMDEfESHKQFLEKQ----------LQSEVERSAQLKTQLLdsEATvRKLNVQVE 492
Cdd:PRK11281   231 YLTARIQRLEHqlqllqeAINSKRLTLSE-KTVQEAQSQDeaariqanplVAQELEINLQLSQRLL--KAT-EKLNTLTQ 306
                          330       340
                   ....*....|....*....|.
gi 2024343403  493 DlKLQLK-------QTQAALE 506
Cdd:PRK11281   307 Q-NLRVKnwldrltQSERNIK 326
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
121-293 7.09e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  121 RESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYE 200
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403  201 LERTHQAKAEALVS----------REKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQR-----------I 259
Cdd:TIGR02168  913 LRRELEELREKLAQlelrleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelgpvnlaaI 992
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2024343403  260 EAFEITQKLQEEKNKTIDDALRrrevAVKNIEET 293
Cdd:TIGR02168  993 EEYEELKERYDFLTAQKEDLTE----AKETLEEA 1022
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
27-54 7.33e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 35.10  E-value: 7.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 2024343403   27 NSLVADHLQRCGYEYSLSVFFPESGLEK 54
Cdd:smart00667   7 NRLILEYLLRNGYEETAETLQKESGLSL 34
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
149-248 8.58e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAEMSQKLqhfKEVEVAKIKMEEKAQTQKEISELRYELERT---HQAKAEALVSREKNAIERLQK 225
Cdd:COG2268   267 AYEIAEANAEREVQRQLEIAERE---REIELQEKEAEREEAELEADVRKPAEAEKQaaeAEAEAEAEAIRAKGLAEAEGK 343
                          90       100
                  ....*....|....*....|...
gi 2024343403 226 QQEIEAKEVYAQRQSLLKDIEVM 248
Cdd:COG2268   344 RALAEAWNKLGDAAILLMLIEKL 366
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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